ID A8NB79_COPC7 Unreviewed; 1086 AA.
AC A8NB79;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Calcium-transporting ATPase 3 {ECO:0000313|EMBL:EAU89725.1};
GN ORFNames=CC1G_07450 {ECO:0000313|EMBL:EAU89725.1};
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU89725.1, ECO:0000313|Proteomes:UP000001861};
RN [1] {ECO:0000313|EMBL:EAU89725.1, ECO:0000313|Proteomes:UP000001861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC {ECO:0000313|Proteomes:UP000001861};
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAU89725.1}.
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DR EMBL; AACS02000009; EAU89725.1; -; Genomic_DNA.
DR RefSeq; XP_001832079.1; XM_001832027.1.
DR AlphaFoldDB; A8NB79; -.
DR STRING; 240176.A8NB79; -.
DR GeneID; 6008563; -.
DR KEGG; cci:CC1G_07450; -.
DR VEuPathDB; FungiDB:CC1G_07450; -.
DR eggNOG; KOG0202; Eukaryota.
DR InParanoid; A8NB79; -.
DR OMA; NMSEVRQ; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000001861; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 3.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 3.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF14; SODIUM TRANSPORT ATPASE 1-RELATED; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 2.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ion transport {ECO:0000256|ARBA:ARBA00023201};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001861};
KW Sodium {ECO:0000256|ARBA:ARBA00023053};
KW Sodium transport {ECO:0000256|ARBA:ARBA00023201};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00023201}.
FT TRANSMEM 88..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 112..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 301..322
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 328..354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 815..836
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 848..867
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 888..920
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 986..1006
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1018..1038
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 34..108
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 500..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1086
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1086 AA; 117185 MW; 7D1D26C036AA002D CRC64;
MAKKTGVELN RRTETTISVT VAPQNPDFFS VTPKSHTLTP ARLAEDLGTS LTDGLSRNEA
ARRLATYGEN VLEGDGGISI WKVLIGQLAN ALTVVLVAAM ALSFGVKDYV EGIVIAVVII
VNTTIGFFQE YRAEKTMDSL RQLSSPTAFV IRNGESVAIP AKDVVPGDLV SIKAGDVVAA
DLRLVSVSNL EISEQLLTGE SVPVAKNVDT YDEDELDIPI GDRLNLCYAS TIVTKGRGVG
IVVGTAMNTQ IGMIAAAIQG KKKSIDEEMA HRPWYHRTLE KIKYIMGLRS GTPLQIKLAK
LAYLLFLFAC LLIIIVFSVA KFKITSEVVL YGIATAIAII PESLVAILTL TMAVGTRKMA
KEHVIVRKLD ALENLGGVTD ICSDKTGTLT LGQMSVQKLW LAADKPHDSE FTAELNDNAL
DPTGIIKRDT DSSVLDGASM PEGVRQAVLV ASLCNVATVR KNLKGQWKST GDPTEVALQV
FSMKLGLGRS TLAPDSLEQE AAAGRPALGE PVPDTDSDAG KAKVQFPAEL SQSKRYELKV
EFPFSSDVKR MTTIYLDKEC ENPKENAIVL IKGAAERILD ASISYIPSPE TNPSQTAPLT
PEVRASFLAK YEELASQGLR VIGLAHRTMP AAELEGLTRE AAEQGFTFLA LAGISDPPRP
ETLGAVRACK AAGIVVHMLT GDHISTARAI AKAVEIIGPD SPPSAVMTAQ EFDKLTDAEV
DALPELPLVI ARCAPDTKVR MIHAGKRRGK HMSMSGDGVN DSPALKLAPV GIAMGMAGSD
VAKDAADLVL TDDNFDSIRV AVSEGRRLFT NIQRFIIHLL AVNVAEVVVL ILGLAFQDEQ
GRSVFPLSPI AILWVNMVTS GPPAFGLGTE KASPDSMLRP PHPLKDGVFS WPVIIDCFAY
GIVMGALSLM TFVIVVWGRY SGELGIECNH SSDAICNTVF RARSATFATL IFDILLFAFE
LKSFDRSVFA LNPNRAWWLE LYENKVLLLS VVGGMVTVVL PIYIPGFNNR VFYQAPIGWE
WGLAIGMTIV FVIWCEVWKI IRKPLFKRWD YGLVQVDPSG EGGTGTAPMA GPSEKQVDEK
ANKVAE
//
